ID J3LNI5_ORYBR Unreviewed; 1310 AA.
AC J3LNI5;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 24-JAN-2024, entry version 66.
DE RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
GN Name=102700691 {ECO:0000313|EnsemblPlants:OB03G26110.1};
OS Oryza brachyantha (malo sina).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX NCBI_TaxID=4533 {ECO:0000313|EnsemblPlants:OB03G26110.1};
RN [1] {ECO:0000313|EnsemblPlants:OB03G26110.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IRGC 101232 {ECO:0000313|EnsemblPlants:OB03G26110.1};
RX PubMed=23481403;
RA Chen J., Huang Q., Gao D., Wang J., Lang Y., Liu T., Li B., Bai Z.,
RA Luis Goicoechea J., Liang C., Chen C., Zhang W., Sun S., Liao Y., Zhang X.,
RA Yang L., Song C., Wang M., Shi J., Liu G., Liu J., Zhou H., Zhou W., Yu Q.,
RA An N., Chen Y., Cai Q., Wang B., Liu B., Min J., Huang Y., Wu H., Li Z.,
RA Zhang Y., Yin Y., Song W., Jiang J., Jackson S.A., Wing R.A., Wang J.,
RA Chen M.;
RT "Whole-genome sequencing of Oryza brachyantha reveals mechanisms underlying
RT Oryza genome evolution.";
RL Nat. Commun. 4:1595-1595(2013).
RN [2] {ECO:0000313|EnsemblPlants:OB03G26110.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (APR-2013) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + phospholipidSide 1 = ADP + phosphate +
CC phospholipidSide 2.; EC=7.6.2.1;
CC Evidence={ECO:0000256|ARBA:ARBA00034036,
CC ECO:0000256|RuleBase:RU362033};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141,
CC ECO:0000256|RuleBase:RU362033}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU362033}.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type IV subfamily. {ECO:0000256|ARBA:ARBA00008109,
CC ECO:0000256|RuleBase:RU362033}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR RefSeq; XP_006650046.1; XM_006649983.2.
DR STRING; 4533.J3LNI5; -.
DR EnsemblPlants; OB03G26110.1; OB03G26110.1; OB03G26110.
DR Gramene; OB03G26110.1; OB03G26110.1; OB03G26110.
DR eggNOG; KOG0206; Eukaryota.
DR HOGENOM; CLU_000846_3_4_1; -.
DR OMA; QALRCGR; -.
DR OrthoDB; 275833at2759; -.
DR Proteomes; UP000006038; Chromosome 3.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0140326; F:ATPase-coupled intramembrane lipid transporter activity; IEA:UniProtKB-EC.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0015914; P:phospholipid transport; IEA:InterPro.
DR CDD; cd02073; P-type_ATPase_APLT_Dnf-like; 1.
DR Gene3D; 3.40.1110.10; Calcium-transporting ATPase, cytoplasmic domain N; 2.
DR Gene3D; 2.70.150.10; Calcium-transporting ATPase, cytoplasmic transduction domain A; 1.
DR Gene3D; 1.20.1110.10; Calcium-transporting ATPase, transmembrane domain; 1.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 2.
DR InterPro; IPR023299; ATPase_P-typ_cyto_dom_N.
DR InterPro; IPR018303; ATPase_P-typ_P_site.
DR InterPro; IPR023298; ATPase_P-typ_TM_dom_sf.
DR InterPro; IPR008250; ATPase_P-typ_transduc_dom_A_sf.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR006539; P-type_ATPase_IV.
DR InterPro; IPR032631; P-type_ATPase_N.
DR InterPro; IPR001757; P_typ_ATPase.
DR InterPro; IPR032630; P_typ_ATPase_c.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR NCBIfam; TIGR01652; ATPase-Plipid; 1.
DR NCBIfam; TIGR01494; ATPase_P-type; 3.
DR PANTHER; PTHR24092:SF148; PHOSPHOLIPID-TRANSPORTING ATPASE; 1.
DR PANTHER; PTHR24092; PROBABLE PHOSPHOLIPID-TRANSPORTING ATPASE; 1.
DR Pfam; PF13246; Cation_ATPase; 1.
DR Pfam; PF16212; PhoLip_ATPase_C; 1.
DR Pfam; PF16209; PhoLip_ATPase_N; 1.
DR PRINTS; PR00119; CATATPASE.
DR SFLD; SFLDG00002; C1.7:_P-type_atpase_like; 1.
DR SFLD; SFLDF00027; p-type_atpase; 1.
DR SUPFAM; SSF81653; Calcium ATPase, transduction domain A; 1.
DR SUPFAM; SSF81665; Calcium ATPase, transmembrane domain M; 1.
DR SUPFAM; SSF56784; HAD-like; 1.
DR SUPFAM; SSF81660; Metal cation-transporting ATPase, ATP-binding domain N; 1.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|RuleBase:RU362033};
KW Magnesium {ECO:0000256|RuleBase:RU362033};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU362033};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU362033};
KW Reference proteome {ECO:0000313|Proteomes:UP000006038};
KW Translocase {ECO:0000256|ARBA:ARBA00022967, ECO:0000256|RuleBase:RU362033};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU362033};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU362033}.
FT TRANSMEM 222..240
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 417..439
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 468..496
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1079..1098
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1110..1131
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1152..1174
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1186..1205
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1212..1234
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1254..1273
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 157..222
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 1043..1283
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 120..153
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 131..152
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1310 AA; 146954 MW; 30196EFBAAFF52A3 CRC64;
MSNGALLLSS SGTSDSPSKH QAPARTSVGS LGCLCQTDSF SSSVYEDCDT ASVNHVDEEE
AVSRVCLVSD VSRGAERFES ADSNFFHRLS VECSQKERQR KVSWGGAMEM QHSPSSLEIG
VVSSSQPQEK PNRSRRVRNK SSQFEDPFSS EHDPRLIYIN DPNRTNDRYE FTGNEIRTSK
YTLITFLPKN LFIQFHRLAY VYFLVIAALN QLPPLAVFGR TASLFPLLFV LFVTAIKDGY
EDWRRHRSDR NENNRETLVL QSGDFRSKTW KNICAGEVVK IHSNETMPCD MVLLSTSDPN
GIAYIQTMNL DGESNLKTRY ARQETMSMII DGSYSGLIKC EQPNRNIYEF TATMELNNQR
IPLGQSNIVL RGCQLKNTEW IVGVVVYAGQ ETKAMLNSTI SPSKSSNLES YMNRETLWLS
AFLLITCSVV ATGMGVWLFR NSKNLDALPY YRRKYFTFGR ENRKDFKFYG IALEIFFSFL
SSVIIFQIMI PISLYITMEL VRVGQSYFMI GDTRMYDSTS GSRFQCRSLN INEDLGQIRY
IFSDKTGTLT QNKMEFRQAS IYGKNYGSSL HVTSDSSFEI SAAESSRQQG SKSKSGVSVD
SALMALLSQP LVGEERLAAH DFFLTLAACN TVIPVSTENS LDLINEINEV GRIDYQGESP
DEQALVTAAS AYGYTLVERT TGHIVVDVQG DRIRLDVLGL HEFDSVRKRM SVVVRFPDNI
VKVLVKGADT SMLSILRRAD DDELHNSSHT KIRESTGNHL SGYSSEGLRT LVIGSKNLTD
AEFSEWQERY EEASTSMTER SAKLRQASAL VECNLTLLGA TGIEDKLQDG VPEAIESLRQ
AGIKVWVLTG DKQETAISIG LSCRLLTQNM HLIIINGSSE FECRRLLADA KAEFGIKSSD
SVRGSRDVCN GDVSKLTTSN GHISEGGIQN FELTGVIASD KLEYSEKVAT FADAELALII
DGSSLVYILE KDLESELFDL ATSCKVVICC RVAPLQKAGI VDLIKSRTSD MTLAIGDGAN
DVSMIQMADV GVGICGQEGR QAVMASDFAM GQFRFLKRLL LVHGHWNYQR IAYMILYNFY
RNAVFVLMLF WYILHTAYSA TLALTDWSSV FYSLIYTSIP TVVVGILDKD LSHNTLLHYP
RLYESGLQNE GYNLTLFWIT MMDTLWQSLV LFYVPFFTYN ISTMDIWSMG SLWTIAVVIL
VNIHLAMDIQ RWVLITHLAV WGSIAATFLC MVLIDSIPIF PNYGTIYNMA ASRTYWLSVC
LIIVLGLLPR FLCKVIYQTF WPSDIQIARE SELLKKLPQR LGSRPTSDII
//
